Ribonuclease E
Ribonuclease E | |||||||||
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Identifiers | |||||||||
EC number | 3.1.26.12 | ||||||||
CAS number | 76106-82-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Ribonuclease E (EC 3.1.26.12, endoribonuclease E, RNase E, Rne protein) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
RNase E is a bacterial ribonuclease that participates in the processing of ribosomal RNA (9S to 5S rRNA) and the chemical degradation of bulk cellular RNA.
References
- ↑ Feng Y, Vickers TA, Cohen SN (November 2002). "The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection". Proceedings of the National Academy of Sciences of the United States of America. 99 (23): 14746–51. doi:10.1073/pnas.202590899. PMC 137490. PMID 12417756.
- ↑ Ehretsmann CP, Carpousis AJ, Krisch HM (January 1992). "Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site". Genes & Development. 6 (1): 149–59. doi:10.1101/gad.6.1.149. PMID 1730408.
- ↑ Cormack RS, Genereaux JL, Mackie GA (October 1993). "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product". Proceedings of the National Academy of Sciences of the United States of America. 90 (19): 9006–10. doi:10.1073/pnas.90.19.9006. PMC 47490. PMID 8415644.
- ↑ Vanzo NF, Li YS, Py B, Blum E, Higgins CF, Raynal LC, Krisch HM, Carpousis AJ (September 1998). "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome". Genes & Development. 12 (17): 2770–81. doi:10.1101/gad.12.17.2770. PMC 317140. PMID 9732274.
- ↑ Steege DA (August 2000). "Emerging features of mRNA decay in bacteria". Rna. 6 (8): 1079–90. doi:10.1017/S1355838200001023. PMC 1369983. PMID 10943888.
- ↑ Callaghan AJ, Grossmann JG, Redko YU, Ilag LL, Moncrieffe MC, Symmons MF, Robinson CV, McDowall KJ, Luisi BF (December 2003). "Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain". Biochemistry. 42 (47): 13848–55. doi:10.1021/bi0351099. PMID 14636052.
External links
- Ribonuclease+E at the US National Library of Medicine Medical Subject Headings (MeSH)
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